1c28

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[[Image:1c28.png|left|200px]]
 
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{{STRUCTURE_1c28| PDB=1c28 | SCENE= }}
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==THE CRYSTAL STRUCTURE OF A COMPLMENT-1Q FAMILY PROTEIN SUGGESTS AN EVOLUTIONARY LINK TO TUMOR NECROSIS FACTOR==
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<StructureSection load='1c28' size='340' side='right'caption='[[1c28]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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===THE CRYSTAL STRUCTURE OF A COMPLMENT-1Q FAMILY PROTEIN SUGGESTS AN EVOLUTIONARY LINK TO TUMOR NECROSIS FACTOR===
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1c28]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C28 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C28 FirstGlance]. <br>
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{{ABSTRACT_PUBMED_9512423}}
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1c28 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c28 OCA], [https://pdbe.org/1c28 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c28 RCSB], [https://www.ebi.ac.uk/pdbsum/1c28 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c28 ProSAT]</span></td></tr>
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==About this Structure==
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</table>
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[[1c28]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C28 OCA].
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== Function ==
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[https://www.uniprot.org/uniprot/ADIPO_MOUSE ADIPO_MOUSE] Important adipokine involved in the control of fat metabolism and insulin sensitivity, with direct anti-diabetic, anti-atherogenic and anti-inflammatory activities. Stimulates AMPK phosphorylation and activation in the liver and the skeletal muscle, enhancing glucose utilization and fatty-acid combustion. Antagonizes TNF-alpha by negatively regulating its expression in various tissues such as liver and macrophages, and also by counteracting its effects. Inhibits endothelial NF-kappa-B signaling through a cAMP-dependent pathway. May play a role in cell growth, angiogenesis and tissue remodeling by binding and sequestering various growth factors with distinct binding affinities, depending on the type of complex, LMW, MMW or HMW.<ref>PMID:11479627</ref> <ref>PMID:11479628</ref> <ref>PMID:12840063</ref> <ref>PMID:15760892</ref> <ref>PMID:15734737</ref>
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==Reference==
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== Evolutionary Conservation ==
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<ref group="xtra">PMID:009512423</ref><references group="xtra"/>
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c2/1c28_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1c28 ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Scherer, P.]]
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[[Category: Scherer P]]
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[[Category: Shapiro, L.]]
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[[Category: Shapiro L]]
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[[Category: Acrp30 c1q tnf trimer all-beta]]
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[[Category: Serum protein]]
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Current revision

THE CRYSTAL STRUCTURE OF A COMPLMENT-1Q FAMILY PROTEIN SUGGESTS AN EVOLUTIONARY LINK TO TUMOR NECROSIS FACTOR

PDB ID 1c28

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